C71Z7_ORYSJ
ID C71Z7_ORYSJ Reviewed; 518 AA.
AC Q6YV88; A0A0P0VKT3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ent-cassadiene hydroxylase {ECO:0000305};
DE EC=1.14.14.69 {ECO:0000269|PubMed:21985968, ECO:0000269|PubMed:25758958};
DE AltName: Full=Cytochrome P450 71Z7;
GN Name=CYP71Z7; OrderedLocusNames=Os02g0570700, LOC_Os02g36190;
GN ORFNames=OsJ_07207, OSJNBa0008E01.37, P0689H05.7;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18759039; DOI=10.1360/02yc9056;
RA Zhong L., Wang K., Tan J., Li W., Li S.;
RT "Putative cytochrome P450 genes in rice genome (Oryza sativa L. ssp.
RT indica) and their EST evidence.";
RL Sci. China, Ser. C, Life Sci. 45:512-517(2002).
RN [7]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21985968; DOI=10.1016/j.febslet.2011.09.038;
RA Wu Y., Hillwig M.L., Wang Q., Peters R.J.;
RT "Parsing a multifunctional biosynthetic gene cluster from rice: Biochemical
RT characterization of CYP71Z6 & 7.";
RL FEBS Lett. 585:3446-3451(2011).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25758958; DOI=10.1007/s00253-015-6496-2;
RA Kitaoka N., Wu Y., Xu M., Peters R.J.;
RT "Optimization of recombinant expression enables discovery of novel
RT cytochrome P450 activity in rice diterpenoid biosynthesis.";
RL Appl. Microbiol. Biotechnol. 99:7549-7558(2015).
CC -!- FUNCTION: Enzyme of the diterpenoid metabolism involved in the
CC biosynthesis of antibacterial oryzalides such as phytocassane
CC (PubMed:21985968). Catalyzes the hydroxylation of ent-cassa-12,15-diene
CC to form ent-3beta-hydroxycassa-12,15-dien-2-one (PubMed:25758958).
CC {ECO:0000269|PubMed:21985968, ECO:0000269|PubMed:25758958}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-cassa-12,15-diene + 3 O2 + 3 reduced [NADPH--hemoprotein
CC reductase] = ent-3beta-hydroxycassa-12,15-dien-2-one + 3 H(+) + 4 H2O
CC + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55480,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:50060,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138970;
CC EC=1.14.14.69; Evidence={ECO:0000269|PubMed:25758958};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for ent-cassadiene {ECO:0000269|PubMed:21985968};
CC Note=kcat is 0.11 sec(-1) with ent-cassadiene as substrate.
CC {ECO:0000269|PubMed:21985968};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Cytochrome P450 Homepage;
CC URL="http://drnelson.uthsc.edu/CytochromeP450.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP005114; BAD17264.1; -; Genomic_DNA.
DR EMBL; AP005835; BAD17678.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09102.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79341.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ23511.1; -; Genomic_DNA.
DR EMBL; AK070167; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015623473.1; XM_015767987.1.
DR AlphaFoldDB; Q6YV88; -.
DR SMR; Q6YV88; -.
DR STRING; 4530.OS02T0570700-01; -.
DR PaxDb; Q6YV88; -.
DR PRIDE; Q6YV88; -.
DR EnsemblPlants; Os02t0570700-01; Os02t0570700-01; Os02g0570700.
DR GeneID; 4329726; -.
DR Gramene; Os02t0570700-01; Os02t0570700-01; Os02g0570700.
DR KEGG; osa:4329726; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_1_1; -.
DR InParanoid; Q6YV88; -.
DR OMA; MIEHKNT; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-18620; -.
DR BRENDA; 1.14.14.69; 8948.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6YV88; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Ent-cassadiene hydroxylase"
FT /id="PRO_0000418865"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 451
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 192
FT /note="S -> G (in Ref. 5; AK070167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57416 MW; 0E389A5318012A9F CRC64;
MEDNKLILAL GLSVLFVLLS KLVSSAMKPR LNLPPGPWTL PLIGSLHHLV MKSPQIHRSL
RALSEKHGPI MQLWMGEVPA VIVSSPAVAE EVLKHQDLRF ADRHLTATIE EVSFGGRDVT
FAPYSERWRH LRKICMQELL TAARVRSFQG VREREVARLV RELAADAGAG GDAGVNLNER
ISKLANDIVM VSSVGGRCSH RDEFLDALEV AKKQITWLSV ADLFPSSKLA RMVAVAPRKG
LASRKRMELV IRRIIQERKD QLMDDSAAGA GEAAAGKDCF LDVLLRLQKE GGTPVPVTDE
IIVVLLFDMF TGASETSPTV LIWILAELMR CPRVMAKAQA EVRQAAVGKT RITENDIVGL
SYLKMVIKEA LRLHSPAPLL NPRKCRETTQ VMGYDIPKGT SVFVNMWAIC RDPNYWEDPE
EFKPERFENN CVDFKGNNFE FLPFGSGRRI CPGINLGLAN LELALASLLY HFDWKLPNGM
LPKDLDMQET PGIVAAKLTT LNMCPVTQIA PSSAEDAS
